ID   XPO4_HUMAN              Reviewed;        1151 AA.
AC   Q9C0E2; Q5VUZ5; Q8N3V6; Q9H934;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2001, sequence version 2.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Exportin-4 {ECO:0000303|PubMed:10944119};
DE            Short=Exp4 {ECO:0000303|PubMed:10944119};
GN   Name=XPO4 {ECO:0000303|PubMed:26787900, ECO:0000312|HGNC:HGNC:17796};
GN   Synonyms=KIAA1721 {ECO:0000303|PubMed:11214970};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA   Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIX. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:347-355(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057823; DOI=10.1038/nature02379;
RA   Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA   Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA   Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA   Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA   Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA   Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA   Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA   Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA   Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA   Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA   Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA   Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA   Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA   Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA   Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA   Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA   Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA   Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA   Rogers J., Ross M.T.;
RT   "The DNA sequence and analysis of human chromosome 13.";
RL   Nature 428:522-528(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 337-1151.
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 888-1151.
RC   TISSUE=Skeletal muscle;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION IN NUCLEAR PROTEIN EXPORT, AND
RP   IDENTIFICATION IN A COMPLEX WITH RAN AND EIF5A.
RX   PubMed=10944119; DOI=10.1093/emboj/19.16.4362;
RA   Lipowsky G., Bischoff F.R., Schwarzmaier P., Kraft R., Kostka S.,
RA   Hartmann E., Kutay U., Goerlich D.;
RT   "Exportin 4: a mediator of a novel nuclear export pathway in higher
RT   eukaryotes.";
RL   EMBO J. 19:4362-4371(2000).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   FUNCTION IN NUCLEAR PROTEIN EXPORT, IDENTIFICATION IN A COMPLEX WITH RAN
RP   AND SMAD3, INTERACTION WITH SMAD3, AND SUBCELLULAR LOCATION.
RX   PubMed=16449645; DOI=10.1128/mcb.26.4.1318-1332.2006;
RA   Kurisaki A., Kurisaki K., Kowanetz M., Sugino H., Yoneda Y., Heldin C.-H.,
RA   Moustakas A.;
RT   "The mechanism of nuclear export of Smad3 involves exportin 4 and Ran.";
RL   Mol. Cell. Biol. 26:1318-1332(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464 AND SER-521, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-464, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [15]
RP   FUNCTION.
RX   PubMed=26787900; DOI=10.1073/pnas.1520045113;
RA   Bhardwaj A., Das S.;
RT   "SIRT6 deacetylates PKM2 to suppress its nuclear localization and oncogenic
RT   functions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:E538-E547(2016).
CC   -!- FUNCTION: Mediates the nuclear export of proteins (cargos), such as
CC       EIF5A, SMAD3 and isoform M2 of PKM (PKM2) (PubMed:10944119,
CC       PubMed:16449645, PubMed:26787900). In the nucleus binds cooperatively
CC       to its cargo and to the GTPase Ran in its active GTP-bound form.
CC       Docking of this trimeric complex to the nuclear pore complex (NPC) is
CC       mediated through binding to nucleoporins (PubMed:10944119,
CC       PubMed:16449645). Upon transit of a nuclear export complex into the
CC       cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to
CC       Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of
CC       the cargo from the export receptor (PubMed:10944119, PubMed:16449645).
CC       XPO4 then return to the nuclear compartment and mediate another round
CC       of transport (PubMed:10944119, PubMed:16449645). The directionality of
CC       nuclear export is thought to be conferred by an asymmetric distribution
CC       of the GTP- and GDP-bound forms of Ran between the cytoplasm and
CC       nucleus (PubMed:10944119, PubMed:16449645). Catalyzes the nuclear
CC       export of hypusinated EIF5A; a small cytoplasmic protein that enters
CC       nucleus and accumulates within nucleolus if not exported back by XPO4
CC       (PubMed:10944119). Specifically mediates nuclear export of isoform M2
CC       of PKM (PKM2) following PKM2 deacetylation by SIRT6 (PubMed:26787900).
CC       Also mediates the nuclear import of SOX transcription factors SRY and
CC       SOX2 (By similarity). {ECO:0000250|UniProtKB:Q9ESJ0,
CC       ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:16449645,
CC       ECO:0000269|PubMed:26787900}.
CC   -!- SUBUNIT: Interacts with Ran and cargo proteins in a GTP-dependent
CC       manner. {ECO:0000269|PubMed:10944119, ECO:0000269|PubMed:16449645}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16449645}. Nucleus
CC       {ECO:0000269|PubMed:16449645}. Note=Shuttles between the nucleus and
CC       the cytoplasm. {ECO:0000269|PubMed:16449645}.
CC   -!- SIMILARITY: Belongs to the exportin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB14409.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB051508; BAB21812.1; -; mRNA.
DR   EMBL; AL512652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL356285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK023108; BAB14409.1; ALT_INIT; mRNA.
DR   EMBL; AL831819; CAD38533.2; -; mRNA.
DR   CCDS; CCDS41872.1; -.
DR   RefSeq; NP_071904.4; NM_022459.4.
DR   AlphaFoldDB; Q9C0E2; -.
DR   SMR; Q9C0E2; -.
DR   BioGRID; 122138; 109.
DR   IntAct; Q9C0E2; 35.
DR   MINT; Q9C0E2; -.
DR   STRING; 9606.ENSP00000255305; -.
DR   TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR   GlyGen; Q9C0E2; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9C0E2; -.
DR   MetOSite; Q9C0E2; -.
DR   PhosphoSitePlus; Q9C0E2; -.
DR   BioMuta; XPO4; -.
DR   DMDM; 17368720; -.
DR   EPD; Q9C0E2; -.
DR   jPOST; Q9C0E2; -.
DR   MassIVE; Q9C0E2; -.
DR   MaxQB; Q9C0E2; -.
DR   PaxDb; 9606-ENSP00000255305; -.
DR   PeptideAtlas; Q9C0E2; -.
DR   ProteomicsDB; 80019; -.
DR   Pumba; Q9C0E2; -.
DR   ABCD; Q9C0E2; 1 sequenced antibody.
DR   Antibodypedia; 41969; 58 antibodies from 20 providers.
DR   DNASU; 64328; -.
DR   Ensembl; ENST00000255305.11; ENSP00000255305.6; ENSG00000132953.18.
DR   GeneID; 64328; -.
DR   KEGG; hsa:64328; -.
DR   MANE-Select; ENST00000255305.11; ENSP00000255305.6; NM_022459.5; NP_071904.4.
DR   UCSC; uc001unq.5; human.
DR   AGR; HGNC:17796; -.
DR   CTD; 64328; -.
DR   DisGeNET; 64328; -.
DR   GeneCards; XPO4; -.
DR   HGNC; HGNC:17796; XPO4.
DR   HPA; ENSG00000132953; Tissue enhanced (skeletal).
DR   MIM; 611449; gene.
DR   neXtProt; NX_Q9C0E2; -.
DR   OpenTargets; ENSG00000132953; -.
DR   PharmGKB; PA134866468; -.
DR   VEuPathDB; HostDB:ENSG00000132953; -.
DR   eggNOG; KOG4541; Eukaryota.
DR   GeneTree; ENSGT00940000153139; -.
DR   HOGENOM; CLU_005818_0_0_1; -.
DR   InParanoid; Q9C0E2; -.
DR   OMA; SKWETNH; -.
DR   OrthoDB; 763157at2759; -.
DR   PhylomeDB; Q9C0E2; -.
DR   TreeFam; TF312991; -.
DR   PathwayCommons; Q9C0E2; -.
DR   SignaLink; Q9C0E2; -.
DR   BioGRID-ORCS; 64328; 23 hits in 1165 CRISPR screens.
DR   ChiTaRS; XPO4; human.
DR   GeneWiki; XPO4; -.
DR   GenomeRNAi; 64328; -.
DR   Pharos; Q9C0E2; Tbio.
DR   PRO; PR:Q9C0E2; -.
DR   Proteomes; UP000005640; Chromosome 13.
DR   RNAct; Q9C0E2; Protein.
DR   Bgee; ENSG00000132953; Expressed in skeletal muscle tissue of rectus abdominis and 151 other cell types or tissues.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005643; C:nuclear pore; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProt.
DR   GO; GO:0005049; F:nuclear export signal receptor activity; IDA:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IDA:UniProt.
DR   GO; GO:0046827; P:positive regulation of protein export from nucleus; IMP:BHF-UCL.
DR   GO; GO:0006611; P:protein export from nucleus; IDA:UniProt.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR014877; XPO1_C_dom.
DR   InterPro; IPR044189; XPO4/7-like.
DR   PANTHER; PTHR12596; EXPORTIN 4,7-RELATED; 1.
DR   PANTHER; PTHR12596:SF1; EXPORTIN-4; 1.
DR   Pfam; PF08767; CRM1_C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   Genevisible; Q9C0E2; HS.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein;
KW   Protein transport; Reference proteome; Transport.
FT   CHAIN           1..1151
FT                   /note="Exportin-4"
FT                   /id="PRO_0000204711"
FT   MOD_RES         464
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976"
FT   MOD_RES         521
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   VARIANT         149
FT                   /note="N -> S (in dbSNP:rs17320607)"
FT                   /id="VAR_048958"
FT   VARIANT         451
FT                   /note="T -> A (in dbSNP:rs9552285)"
FT                   /id="VAR_048959"
FT   CONFLICT        511
FT                   /note="L -> S (in Ref. 3; BAB14409)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1151 AA;  130139 MW;  38E7EEFC938B07C5 CRC64;
     MMAAALGPPE VIAQLENAAK VLMAPPSMVN NEQRQHAEHI FLSFRKSKSP FAVCKHILET
     SKVDYVLFQA ATAIMEAVVR EWILLEKGSI ESLRTFLLTY VLQRPNLQKY VREQILLAVA
     VIVKRGSLDK SIDCKSIFHE VSQLISSGNP TVQTLACSIL TALLSEFSSS SKTSNIGLSM
     EFHGNCKRVF QEEDLRQIFM LTVEVLQEFS RRENLNAQMS SVFQRYLALA NQVLSWNFLP
     PNLGRHYIAM FESSQNVLLK PTESWRETLL DSRVMELFFT VHRKIREDSD MAQDSLQCLA
     QLASLHGPIF PDEGSQVDYL AHFIEGLLNT INGIEIEDSE AVGISSIISN LITVFPRNVL
     TAIPSELFSS FVNCLTHLTC SFGRSAALEE VLDKDDMVYM EAYDKLLESW LTLVQDDKHF
     HKGFFTQHAV QVFNSYIQCH LAAPDGTRNL TANGVASREE EEISELQEDD RDQFSDQLAS
     VGMLGRIAAE HCIPLLTSLL EERVTRLHGQ LQRHQQQLLA SPGSSTVDNK MLDDLYEDIH
     WLILVTGYLL ADDTQGETPL IPPEIMEYSI KHSSEVDINT TLQILGSPGE KASSIPGYNR
     TDSVIRLLSA ILRVSEVESR AIRADLTHLL SPQMGKDIVW FLKRWAKTYL LVDEKLYDQI
     SLPFSTAFGA DTEGSQWIIG YLLQKVISNL SVWSSEQDLA NDTVQLLVTL VERRERANLV
     IQCENWWNLA KQFASRSPPL NFLSSPVQRT LMKALVLGGF AHMDTETKQQ YWTEVLQPLQ
     QRFLRVINQE NFQQMCQQEE VKQEITATLE ALCGIAEATQ IDNVAILFNF LMDFLTNCIG
     LMEVYKNTPE TVNLIIEVFV EVAHKQICYL GESKAMNLYE ACLTLLQVYS KNNLGRQRID
     VTAEEEQYQD LLLIMELLTN LLSKEFIDFS DTDEVFRGHE PGQAANRSVS AADVVLYGVN
     LILPLMSQDL LKFPTLCNQY YKLITFICEI FPEKIPQLPE DLFKSLMYSL ELGMTSMSSE
     VCQLCLEALT PLAEQCAKAQ ETDSPLFLAT RHFLKLVFDM LVLQKHNTEM TTAAGEAFYT
     LVCLHQAEYS ELVETLLSSQ QDPVIYQRLA DAFNKLTASS TPPTLDRKQK MAFLKSLEEF
     MANVGGLLCV K
//